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Reshaping of the conformational search of a protein by the chaperone trigger factor

Alireza Mashaghi, Günter Kramer, Philipp Bechtluft, Beate Zachmann-Brand, Arnold J. M. Driessen, Bernd Bukau and Sander J. Tans ()
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Alireza Mashaghi: FOM institute AMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands
Günter Kramer: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, Heidelberg 69120, Germany
Philipp Bechtluft: FOM institute AMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands
Beate Zachmann-Brand: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, Heidelberg 69120, Germany
Arnold J. M. Driessen: Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 7, 9749 AG Groningen, The Netherlands
Bernd Bukau: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, Heidelberg 69120, Germany
Sander J. Tans: FOM institute AMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

Nature, 2013, vol. 500, issue 7460, 98-101

Abstract: The bacterial chaperone named trigger factor is found to stabilize protein folding intermediates that eventually convert to the native state, suggesting that chaperones play a direct role in instructing protein folding.

Date: 2013
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DOI: 10.1038/nature12293

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